Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person Stimulation of platelets with collagen-related peptide leads...
| Class:Id | Summation:429448 |
|---|---|
| _displayName | Stimulation of platelets with collagen-related peptide leads... |
| _timestamp | 2017-12-08 14:47:08 |
| created | [InstanceEdit:429457] Jupe, S, 2009-07-15 |
| literatureReference | [LiteratureReference:481047] Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function [LiteratureReference:481039] Adaptors as central mediators of signal transduction in immune cells [LiteratureReference:434845] Differential requirement for LAT and SLP-76 in GPVI versus T cell receptor signaling [LiteratureReference:429444] SLP76 and SLP65: complex regulation of signalling in lymphocytes and beyond [LiteratureReference:429456] Fetal hemorrhage and platelet dysfunction in SLP-76-deficient mice [LiteratureReference:434742] Hematopoietic reconstitution of SLP-76 corrects hemostasis and platelet signaling through alpha IIb beta 3 and collagen receptors |
| modified | [InstanceEdit:434725] Jupe, S, 2009-09-02 [InstanceEdit:481043] Jupe, S, 2010-01-27 [InstanceEdit:9032138] Orlic-Milacic, Marija, 2017-12-06 [InstanceEdit:9032254] Orlic-Milacic, Marija, 2017-12-08 |
| text | Stimulation of platelets with collagen-related peptide leads to tyrosine phosphorylation of SLP-76, an adaptor protein with multiple binding domains (Gross et al. 1999). Phosphorylation of SLP-76 is mediated by Syk, analogous to the role of ZAP-70 in phosphorylating T-cell SLP-76 (Bubeck-Wardenberg et al. 1996, Hussain et al. 1999, Fasbender et al. 2017). SLP-76 was shown to bind to tyrosine-phosphorylated C-terminal tail of SYK (de Castro et al. 2012). The phosphorylated tyrosine residues provide a binding site for the SH2 domains of downstream signalling proteins like Vav, Itk and ADAP (Jordan et al. 2003). Platelets from mice defective in SLP76 do not connect GPVI engagement with downstream signaling (Clements et al. 1999, Judd et al. 2000). GPVI signaling via SLP-76 does not appear to require LAT or GADS (Judd et al. 2002) suggesting that the mechanism is not identical to that of T-cells. LAT and SLP-76 are both required for P-selectin expression and degranulation but may function independently, or rely on proteins not required by T-cells (Jordan et al. 2003). |
| (summation) | [Reaction:429449] Syk activation leads to SLP-76 activation [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by Stimulation of platelets with collagen-related peptide leads... (429448)
